beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ...
71-447
5.28e-128
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340861 [Multi-domain] Cd Length: 364 Bit Score: 375.50 E-value: 5.28e-128
Monogalactosyldiacylglycerol (MGDG) synthase; This family represents a conserved region of ...
82-250
8.03e-78
Monogalactosyldiacylglycerol (MGDG) synthase; This family represents a conserved region of approximately 180 residues within plant and bacterial monogalactosyldiacylglycerol (MGDG) synthase (EC:2.4.1.46). In Arabidopsis, there are two types of MGDG synthase which differ in their N-terminal portion: type A and type B.
Pssm-ID: 284368 Cd Length: 169 Bit Score: 239.96 E-value: 8.03e-78
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440471 [Multi-domain] Cd Length: 363 Bit Score: 68.23 E-value: 1.85e-12
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ...
71-447
5.28e-128
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340861 [Multi-domain] Cd Length: 364 Bit Score: 375.50 E-value: 5.28e-128
Monogalactosyldiacylglycerol (MGDG) synthase; This family represents a conserved region of ...
82-250
8.03e-78
Monogalactosyldiacylglycerol (MGDG) synthase; This family represents a conserved region of approximately 180 residues within plant and bacterial monogalactosyldiacylglycerol (MGDG) synthase (EC:2.4.1.46). In Arabidopsis, there are two types of MGDG synthase which differ in their N-terminal portion: type A and type B.
Pssm-ID: 284368 Cd Length: 169 Bit Score: 239.96 E-value: 8.03e-78
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440471 [Multi-domain] Cd Length: 363 Bit Score: 68.23 E-value: 1.85e-12
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.
Pssm-ID: 340818 [Multi-domain] Cd Length: 350 Bit Score: 64.16 E-value: 3.96e-11
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ...
311-396
1.29e-03
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.
Pssm-ID: 427711 [Multi-domain] Cd Length: 166 Bit Score: 39.62 E-value: 1.29e-03
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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